2021
Tissue-specific dynamic codon redefinition in Drosophila
Hudson AM, Szabo NL, Loughran G, Wills NM, Atkins JF, Cooley L. Tissue-specific dynamic codon redefinition in Drosophila. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2012793118. PMID: 33500350, PMCID: PMC7865143, DOI: 10.1073/pnas.2012793118.Peer-Reviewed Original ResearchConceptsStop codonTranslational stop codon readthroughReadthrough efficiencyHuman tissue culture cellsStop codon readthroughTissue-specific regulationAdult central nervous system (CNS) tissueTissue culture cellsReadthrough productKelch proteinUbiquitin ligaseSingle geneAdult brainIndividual proteinsCodon readthroughReadthroughViral mRNAsC-terminalMalpighian tubulesCodonNeuronal proteinsCell typesAmino acidsCulture cellsDrosophila
2020
HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis
Gerdes JA, Mannix KM, Hudson AM, Cooley L. HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis. Genetics 2020, 216: 717-734. PMID: 32883702, PMCID: PMC7648574, DOI: 10.1534/genetics.120.303629.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAnimalsCalmodulin-Binding ProteinsCytokinesisDrosophila melanogasterDrosophila ProteinsFemaleFilaminsOogenesisOvumConceptsGermline ring canalsRing canalsActin cytoskeletonF-actinDrosophila melanogaster oogenesisSomatic follicle cellsCombination of CRISPRF-actin accumulationF-actin recruitmentFilamentous actin cytoskeletonFemale germlineActin structuresFruit flyHigh fecundityFollicle cellsCytoskeletonGermlineOverexpressionAccumulationDrosophilaOogenesisMutagenesisCRISPRFilaminGenes
2018
Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion
Hudson AM, Mannix KM, Gerdes JA, Kottemann MC, Cooley L. Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion. Development 2018, 146: dev169219. PMID: 30559276, PMCID: PMC6340150, DOI: 10.1242/dev.169219.Peer-Reviewed Original ResearchConceptsTandem affinity purificationUbiquitin ligase complexCullin-3 functionShort sequence motifsSpecialized cytoskeletal structuresUbiquitin-proteasome systemF-actin cytoskeletonSpecialized actinLigase complexActin cytoskeletonRing canalsSequence motifsGenetic evidenceCytoskeletal structuresAffinity purificationCytoskeletonSubstrate degradationBiochemical evidenceUnusual mechanismKelchCRL3CullinMass spectrometryOogenesisMutagenesis
2015
Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase
Hudson AM, Mannix KM, Cooley L. Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase. Genetics 2015, 201: 1117-1131. PMID: 26384358, PMCID: PMC4649639, DOI: 10.1534/genetics.115.181289.Peer-Reviewed Original ResearchConceptsKelch functionE3 ligaseCullin-RING E3 ligaseGermline ring canalsActin cytoskeletal organizationDrosophila kelch proteinUbiquitin ligase activityCross-link F-actinUbiquitin E3 ligaseRing canalsKelch proteinProtein substratesCytoskeletal defectsCytoskeletal organizationCytoskeletal remodelingLigase activityCullin 3KelchF-actinCytoskeletonLigaseProteasomeVivoCul3Mutagenesis
2014
Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers
Burn KM, Shimada Y, Ayers K, Vemuganti S, Lu F, Hudson A, Cooley L. Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers. Developmental Biology 2014, 398: 206-217. PMID: 25481758, PMCID: PMC4340711, DOI: 10.1016/j.ydbio.2014.11.021.Peer-Reviewed Original ResearchConceptsDrosophila insulin-like peptidesEgg chambersStarvation responseBody organizationDrosophila egg chamberMotor protein dyneinNutrient-rich conditionsPoor nutrient availabilityInsulin-like peptidesProcessing bodiesDrosophila femalesGermline cellsP-bodiesNutrient availabilityDynein activityInsulin signalingProgeny survivalInsulin pathwayKinesin activityFollicle cellsMicrotubulesStarvationBovine insulinPotential mechanismsProtective responseA Regulatory Network of Drosophila Germline Stem Cell Self-Renewal
Yan D, Neumüller RA, Buckner M, Ayers K, Li H, Hu Y, Yang-Zhou D, Pan L, Wang X, Kelley C, Vinayagam A, Binari R, Randklev S, Perkins LA, Xie T, Cooley L, Perrimon N. A Regulatory Network of Drosophila Germline Stem Cell Self-Renewal. Developmental Cell 2014, 28: 459-473. PMID: 24576427, PMCID: PMC3998650, DOI: 10.1016/j.devcel.2014.01.020.Peer-Reviewed Original ResearchConceptsGermline stem cellsSelf-renewal factorsDrosophila female germline stem cellsStem cellsDifferent stem cell lineagesLarge-scale RNAi screenFemale germline stem cellsLoss of Set1Stem Cell Self-RenewalSpecific genetic networksHistone methyltransferase Set1Stem cell identityCell fate decisionsStem cell lineagesCell Self-RenewalSelf-renewal genesRNAi screenDistinct fatesFate decisionsGSC maintenanceCell identityCell fateRegulatory networksGenetic networksNeural stem cells
2013
Bridging the divide
McLean PF, Cooley L. Bridging the divide. Fly 2013, 8: 13-18. PMID: 24406334, PMCID: PMC3974888, DOI: 10.4161/fly.27016.Peer-Reviewed Original ResearchConceptsRing canalsMitotic clonesSomatic tissuesDrosophila somatic tissuesFollicle cellsProtein of interestNon-recombined cellsDirect cytoplasmic connectionsDrosophila oogenesisImaginal discsGenetic toolsIntercellular exchangeProtein movementCleavage furrowCytoplasmic connectionsProteinClonesCellsMosaic cellsClonal dataOogenesisGFPTissueProtein Equilibration Through Somatic Ring Canals in Drosophila
McLean PF, Cooley L. Protein Equilibration Through Somatic Ring Canals in Drosophila. Science 2013, 340: 1445-1447. PMID: 23704373, PMCID: PMC3819220, DOI: 10.1126/science.1234887.Peer-Reviewed Original ResearchConceptsRing canalsLarval imaginal discsDrosophila ovaryClone boundariesImaginal discsIncomplete cytokinesisIntercellular communicationCytoplasmic contentsFollicle cellsIntercellular bridgesTissue biologyProtein expressionConnected cellsDrosophilaCytokinesisCellsBiologyProteinTissueExpressionOvaries
2011
Intercellular protein movement in syncytial Drosophila follicle cells
Airoldi SJ, McLean PF, Shimada Y, Cooley L. Intercellular protein movement in syncytial Drosophila follicle cells. Journal Of Cell Science 2011, 124: 4077-4086. PMID: 22135360, PMCID: PMC3244987, DOI: 10.1242/jcs.090456.Peer-Reviewed Original ResearchConceptsImaginal disc cellsRing canalsFollicle cellsPavarotti kinesin-like proteinDrosophila follicle cellsIntercellular protein movementEgg chamber developmentKinesin-like proteinMitotic cleavage furrowsLive-cell confocal microscopyDisc cellsBroad functional significanceDrosophila germlineGermline cellsCytoplasmic proteinsSomatic cellsProtein movementCleavage furrowFunctional significanceChamber developmentSyncytial organizationConfocal microscopyGermlineProteinCellsReversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis
Shimada Y, Burn KM, Niwa R, Cooley L. Reversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis. Developmental Biology 2011, 355: 250-262. PMID: 21570389, PMCID: PMC3118931, DOI: 10.1016/j.ydbio.2011.04.022.Peer-Reviewed Original ResearchConceptsEgg chambersNutrient stressIntercellular transportMT reorganizationNutrient availabilityNurse cellsPutative RNA binding proteinMT-dependent mannerRNA binding proteinYpsilon SchachtelDrosophila oogenesisProcessing bodiesProtein localizationEarly oogenesisNutrient deprivationMicrotubule organizationMetabolic checkpointCytoplasmic componentsAnimal oocytesStress responseYolk uptakeBinding proteinPrevitellogenic stageOogenesisIndependent mechanisms
2010
Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton
Hudson AM, Cooley L. Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton. Journal Of Cell Biology 2010, 188: 29-37. PMID: 20065088, PMCID: PMC2812842, DOI: 10.1083/jcb.200909017.Peer-Reviewed Original ResearchConceptsDrosophila KelchCullin 3Cullin-RING ubiquitin E3 ligasesGermline ring canalsSubstrate adaptor proteinCullin-RING ligaseDiverse protein familiesF-actin cytoskeletal structureUbiquitin E3 ligasesProtein ubiquitylationActin cytoskeletonE3 ligasesRing canalsAdaptor proteinProtein familySequence motifsCytoskeletal structuresFilamentous actinKelchProteinUbiquitylationLigasesCytoskeletonLigaseRepeats
2007
Jagunal is required for reorganizing the endoplasmic reticulum during Drosophila oogenesis
Lee S, Cooley L. Jagunal is required for reorganizing the endoplasmic reticulum during Drosophila oogenesis. Journal Of Cell Biology 2007, 176: 941-952. PMID: 17389229, PMCID: PMC2064080, DOI: 10.1083/jcb.200701048.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCell DifferentiationConserved SequenceCytoplasmic StreamingDrosophila melanogasterDrosophila ProteinsEndoplasmic ReticulumExocytosisGolgi ApparatusMembrane ProteinsMicroscopy, Electron, TransmissionMolecular Sequence DataOocytesOogenesisProtein TransportSequence Homology, Amino AcidSequence Homology, Nucleic AcidTransport VesiclesZebrafishConceptsVesicular trafficMembrane trafficEndoplasmic reticulumER reorganizationER membrane proteinsDrosophila melanogaster oocytesDrosophila oogenesisMembrane proteinsOocyte endoplasmic reticulumLateral membranesER clusteringReticulumImportant mechanismVitellogenesisOocytesOogenesisEndocytosisReorganizationProteinMembraneCellsExploring Strategies for Protein Trapping in Drosophila
Quiñones-Coello A, Petrella LN, Ayers K, Melillo A, Mazzalupo S, Hudson AM, Wang S, Castiblanco C, Buszczak M, Hoskins RA, Cooley L. Exploring Strategies for Protein Trapping in Drosophila. Genetics 2007, 175: 1089-1104. PMID: 17179094, PMCID: PMC1840052, DOI: 10.1534/genetics.106.065995.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein trapEnhancer trapFluorescent proteinExpression dataGFP expressionGFP fusion proteinFluorescent protein tagsCell biological studiesProduction of GFPWeb-accessible databaseChromosomal positionProtein tagsProtein trappingEndogenous proteinsGenomic DNASplice acceptorDonor sequenceNew insertionsMolecular informationGenesProteinDrosophilaTransposonBiological studiesThe Ovhts polyprotein is cleaved to produce fusome and ring canal proteins required for Drosophila oogenesis
Petrella LN, Smith-Leiker T, Cooley L. The Ovhts polyprotein is cleaved to produce fusome and ring canal proteins required for Drosophila oogenesis. Development 2007, 134: 703-712. PMID: 17215303, DOI: 10.1242/dev.02766.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCalmodulin-Binding ProteinsDrosophilaDrosophila ProteinsFemaleMultiprotein ComplexesOocytesOogenesisOvaryPolyproteinsConceptsDrosophila oogenesisRing canalsFemale sterile mutantPost-mitotic cellsDrosophila adducinSpecialized organellesEarly oogenesisLate oogenesisHT proteinsFusomeMitotic proliferationHT genesMitotic cellsOogenesisGerm cellsNormal developmentCell proliferationProteinPolyproteinCellsEssential componentProliferationMutantsAdducinOrganelles
2006
Illuminating the role of caspases during Drosophila oogenesis
Mazzalupo S, Cooley L. Illuminating the role of caspases during Drosophila oogenesis. Cell Death & Differentiation 2006, 13: 1950-1959. PMID: 16528381, DOI: 10.1038/sj.cdd.4401892.Peer-Reviewed Original ResearchConceptsNurse cell deathCaspase activityCell deathNurse cellsFluorescent proteinApoptosis protein 1Caspase inhibitor p35Caspase cleavage siteStarvation-induced deathRole of caspasesStarvation-induced apoptosisCyan fluorescent proteinYellow fluorescent proteinDrosophila inhibitorGermline developmentDrosophila oogenesisNormal oogenesisPoor environmental conditionsOogenesisCleavage siteProtein 1Environmental conditionsCaspasesProteinOocytes
2002
Arp2/3-Dependent Psuedocleavage Furrow Assembly in Syncytial Drosophila Embryos
Stevenson V, Hudson A, Cooley L, Theurkauf WE. Arp2/3-Dependent Psuedocleavage Furrow Assembly in Syncytial Drosophila Embryos. Current Biology 2002, 12: 705-711. PMID: 12007413, DOI: 10.1016/s0960-9822(02)00807-2.Peer-Reviewed Original ResearchConceptsDrosophila embryosPseudocleavage furrowsCell cycleActin capActin reorganizationSomatic cell divisionLocal actin polymerizationSyncytial Drosophila embryosARPC1 subunitArp2/3 complexNuclear positioningEmbryonic divisionsComplex localizeCell divisionActin polymerizationCleavage furrowFurrow formationCap functionSpindle fusionMolecular mechanismsArp2/3EmbryosVivo analysisMutationsAssemblyDcas Is Required for importin-α3 Nuclear Export and Mechano-Sensory Organ Cell Fate Specification in Drosophila
Tekotte H, Berdnik D, Török T, Buszczak M, Jones LM, Cooley L, Knoblich JA, Davis I. Dcas Is Required for importin-α3 Nuclear Export and Mechano-Sensory Organ Cell Fate Specification in Drosophila. Developmental Biology 2002, 244: 396-406. PMID: 11944946, DOI: 10.1006/dbio.2002.0612.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAlpha KaryopherinsAnimalsApoptosisCellular Apoptosis Susceptibility ProteinDNA HelicasesDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianGene Expression Regulation, DevelopmentalIn Situ HybridizationMechanoreceptorsMorphogenesisPhylogenyRNA, MessengerSense OrgansConceptsNuclear exportEmbryonic central nervous systemNuclear protein importCell fate specificationSpecific developmental phenotypesHuman genetic disordersProtein importDrosophila orthologImportin alphaFate specificationExport receptorCell identityDevelopmental phenotypesHypomorphic alleleEmbryonic cellsVivo functionNotch pathwayTissue specificityCytoplasmic distributionEpidermal cellsDifferent tissuesCharacteristics of mutationsGenetic disordersMutationsPhenotypeMutations in the midway Gene Disrupt a Drosophila Acyl Coenzyme A: Diacylglycerol Acyltransferase
Buszczak M, Lu X, Segraves WA, Chang TY, Cooley L. Mutations in the midway Gene Disrupt a Drosophila Acyl Coenzyme A: Diacylglycerol Acyltransferase. Genetics 2002, 160: 1511-1518. PMID: 11973306, PMCID: PMC1462074, DOI: 10.1093/genetics/160.4.1511.Peer-Reviewed Original ResearchConceptsEgg chambersDiacylglycerol acyltransferaseNurse cellsAcyl coenzyme AMutant egg chambersNurse cell deathCell deathInsect cells resultsEgg chamber developmentCoenzyme AGermline apoptosisDrosophila oogenesisCytoplasm transportDGAT activityCells resultsChamber developmentNeutral lipidsGenesLipid metabolismDiacylglycerolApoptosisAcyltransferaseDrosophilaCellsOogenesisControl of DNA Replication and Chromosome Ploidy by Geminin and Cyclin A
Mihaylov IS, Kondo T, Jones L, Ryzhikov S, Tanaka J, Zheng J, Higa LA, Minamino N, Cooley L, Zhang H. Control of DNA Replication and Chromosome Ploidy by Geminin and Cyclin A. Molecular And Cellular Biology 2002, 22: 1868-1880. PMID: 11865064, PMCID: PMC135598, DOI: 10.1128/mcb.22.6.1868-1880.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell LineCell NucleusCheckpoint Kinase 1ChromosomesCyclin ACyclin BDNADNA ReplicationDNA-Binding ProteinsDown-RegulationDrosophilaDrosophila ProteinsFlow CytometryGene SilencingMolecular Sequence DataPloidiesProtein Kinase InhibitorsProtein KinasesRNA, Double-StrandedSequence Homology, Amino AcidConceptsDNA replicationGeminin deficiencyGenome stabilityCyclin ASingle giant nucleusGiant nucleiCell cycle arrestDrosophila homologueDrosophila cellsGenome instabilityCheckpoint controlChromosome ploidyReplication factorsOverreplicationCyclin BGemininDouble knockoutCycle arrestRapid downregulationDNA contentGenomeSilencingEffect of cyclinHomologuesCyclinDrosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation
Kelso RJ, Hudson AM, Cooley L. Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation. Journal Of Cell Biology 2002, 156: 703-713. PMID: 11854310, PMCID: PMC2174084, DOI: 10.1083/jcb.200110063.Peer-Reviewed Original ResearchMeSH KeywordsActinsAlanineAmino Acid SequenceAnimalsCarrier ProteinsCross-Linking ReagentsDrosophilaDrosophila ProteinsFemaleInsect ProteinsMicrofilament ProteinsMicroscopy, ElectronMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationProtein-Tyrosine KinasesProto-Oncogene ProteinsRecombinant Fusion ProteinsSequence Homology, Amino AcidSignal TransductionTyrosineConceptsRing canalsActin organizationDrosophila kelch geneOvarian ring canalsRing canal growthActin cross-linking activitySite-directed mutagenesisTwo-dimensional electrophoresisActin binding siteKelch functionDrosophila KelchCross-linking activityProper morphogenesisKelch proteinTyrosine phosphorylationKelch geneNegative regulationRepeat 5KelchActin filamentsResidue 627Biochemical studiesCanal growthProteinMutants